ReviewCurrent opinion in cell biology2009
Translocation of proteins through the Sec61 and SecYEG channels.
Review in Current opinion in cell biology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
26 citing papers in PubMed, 44 citations in OpenAlex.
- Article
- Sec61β maintains cytoplasmic proteostasis via ARIH1-mediated translational repression upon ER stress.EMBO reports · 2026Article
- Inhibitors of the Sec61 Complex and Novel High Throughput Screening Strategies to Target the Protein Translocation Pathway.International journal of molecular sciences · 2021Review
- Cancer associated mutations in Sec61γ alter the permeability of the ER translocase.PLoS genetics · 2021Article
- Responses to chemical cross-talk between the Mycobacterium ulcerans toxin, mycolactone, and Staphylococcus aureus.Scientific reports · 2021Article
- Reprogramming of sugar transport pathways in Escherichia coli using a permeabilized SecY protein-translocation channel.Biotechnology and bioengineering · 2020Article
- The Sec61/SecY complex is inherently deficient in translocating intrinsically disordered proteins.The Journal of biological chemistry · 2017Article
- Anionic Phospholipids and the Albino3 Translocase Activate Signal Recognition Particle-Receptor Interaction during Light-harvesting Chlorophyll a/b-binding Protein Targeting.The Journal of biological chemistry · 2017Article
- Breaking the bacterial protein targeting and translocation model: oral organisms as a case in point.Molecular oral microbiology · 2015Review
- Illumination of growth, division and secretion by metabolic labeling of the bacterial cell surface.FEMS microbiology reviews · 2015Review
- Transcriptional regulation of secretory capacity by bZip transcription factors.Frontiers in biology · 2015Article
- Co-translational protein targeting to the bacterial membrane.Biochimica et biophysica acta · 2014Review
- Cotranslational folding inhibits translocation from within the ribosome-Sec61 translocon complex.Nature structural & molecular biology · 2014Article
- Glycolipozyme MPIase is essential for topology inversion of SecG during preprotein translocation.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- The mitochondrial oxidase assembly protein1 (Oxa1) insertase forms a membrane pore in lipid bilayers.The Journal of biological chemistry · 2012Article
- Protein secretion and the endoplasmic reticulum.Cold Spring Harbor perspectives in biology · 2012Review
- Functional implementation of the posttranslational SecB-SecA protein-targeting pathway in Bacillus subtilis.Applied and environmental microbiology · 2012Article
- Secretory protein profiling reveals TNF-α inactivation by selective and promiscuous Sec61 modulators.Chemistry & biology · 2011Article
- Translocation channel gating kinetics balances protein translocation efficiency with signal sequence recognition fidelity.Molecular biology of the cell · 2011Article
- Free energy of nascent-chain folding in the translocon.Journal of the American Chemical Society · 2011Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
The Sec61 and SecYEG translocation channels mediate the selective transport of proteins across the endoplasmic reticulum and bacterial inner membrane, respectively. These channels are also responsible for the integration of membrane proteins. To accomplish these two critical events in protein expression, the transport channels undergo conformational changes to permit the export of lumenal domains and the integration of transmembrane spans. Novel insight into how these channels open during protein translocation has been provided by a combination of the analysis of new channel structures, biochemical characterization of translocation intermediates, molecular dynamics simulations, and in vivo and in vitro analysis of structure-based Sec61 and SecY mutants.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.